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PMID: 10409759 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The cleavage and polyadenylation specificity factor in Xenopus laevis oocytes is a cytoplasmic factor involved in regulated polyadenylation.

Molecular and cellular biology ·Vol. 19 ·No. 8 ·1999-08-00 ·Pages 5707-17

Dickson KS, Bilger A, Ballantyne S, Wickens MP

Abstract

During early development, specific mRNAs receive poly(A) in the cytoplasm. This cytoplasmic polyadenylation reaction correlates with, and in some cases causes, translational stimulation. Previously, it was suggested that a factor similar to the multisubunit nuclear cleavage and polyadenylation specificity factor (CPSF) played a role in cytoplasmic polyadenylation. A cDNA encoding a cytoplasmic form of the 100-kDa subunit of Xenopus laevis CPSF has now been isolated. The protein product is 91% identical at the amino acid sequence level to nuclear CPSF isolated from Bos taurus thymus. This report provides three lines of evidence that implicate the X. laevis homologue of the 100-kDa subunit of CPSF in the cytoplasmic polyadenylation reaction. First, the protein is predominantly localized to the cytoplasm of X. laevis oocytes. Second, the 100-kDa subunit of X. laevis CPSF forms a specific complex with RNAs that contain both a cytoplasmic polyadenylation element (CPE) and the polyadenylation element AAUAAA. Third, immunodepletion of the 100-kDa subunit of X. laevis CPSF reduces CPE-specific polyadenylation in vitro. Further support for a cytoplasmic form of CPSF comes from evidence that a putative homologue of the 30-kDa subunit of nuclear CPSF is also localized to the cytoplasm of X. laevis oocytes. Overexpression of influenza virus NS1 protein, which inhibits nuclear polyadenylation through an interaction with the 30-kDa subunit of nuclear CPSF, prevents cytoplasmic polyadenylation, suggesting that the cytoplasmic X. laevis form of the 30-kDa subunit of CPSF is involved in this reaction. Together, these results indicate that a distinct, cytoplasmic form of CPSF is an integral component of the cytoplasmic polyadenylation machinery.

MeSH Terms
Amino Acid Sequence Animals Cattle Cell Nucleus/metabolism Cytoplasm/metabolism Macromolecular Substances Molecular Sequence Data Oocytes/metabolism RNA Precursors/metabolism RNA Processing, Post-Transcriptional/physiology RNA, Messenger/biosynthesis RNA-Binding Proteins/genetics,isolation & purification,physiology Sequence Alignment Sequence Homology, Amino Acid Transcription Factors/physiology Viral Nonstructural Proteins/genetics,physiology Xenopus Proteins Xenopus laevis/genetics,metabolism mRNA Cleavage and Polyadenylation Factors
Chemicals
Cpeb1 protein, Xenopus INS1 protein, influenza virus Macromolecular Substances RNA Precursors RNA, Messenger RNA-Binding Proteins Transcription Factors Viral Nonstructural Proteins Xenopus Proteins mRNA Cleavage and Polyadenylation Factors
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Dickson K S
Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisconsin 53706, USA.
Bilger A
Ballantyne S
Wickens M P
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/MCB.19.8.5707
Published
1999-08-00
Pages
5707-17
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC84422
Subset
IM
Grants
NIGMS NIH HHS · GM50942 · United States
NIGMS NIH HHS · R01 GM050942 · United States
NIGMS NIH HHS · R37 GM031892 · United States
NIGMS NIH HHS · GM31892 · United States
NIGMS NIH HHS · R01 GM031892 · United States
Databases
GENBANK
AF139986
External Links
PubMed source DOI: 10.1128/MCB.19.8.5707 PMC Full Text View journal details
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